مشخصات پژوهش

عنوان	Scopoletin and Morin Inhibit Lactate Dehydrogenase Enzyme Activity, Which Is Critical for Cancer Metabolism
نوع پژوهش	مقاله چاپ شده
کلیدواژه‌ها	Lactate Dehydrogenase, Morin, Scopoletin, Spectrophotometry, Enzyme inhibitors
چکیده	Background: Lactate dehydrogenase (LDH) is a tetrameric enzyme that catalyzes the interconversion of pyruvate to L-lactate. The importance of this enzyme is because LDH isoenzymes are involved in cancer, heart, and liver diseases. Inhibition of this enzyme can help prevent and treat different diseases. Morin is a flavonoid found in the Moraceae family and scopoletin is a coumarin found in Scopolia genus. Objectives: The aim of this study was to determine the effect of morin and scopoletin as two natural products on the activity and structure of lactate dehydrogenase enzyme. Methods: Morin and scopoletin were examined for inhibition of the activity of LDH in 100mMsodium phosphate buffer pH 7.5, at room temperature using UV-V spectrophotometry. Fluorescence spectroscopy was used to characterize protein structural changes in the presence of morin and scopoletin. Results: Km and Vmax of LDH for pyruvate were 11.69 mM and 1.258 mM/min, respectively. The kinetic results showed that morin and scopoletin are LDH inhibitors. The Ki values of morin and scopoletin were determined as 1.78 M and 0.8 M, respectively, using a secondary plot. Fluorescence intensity quenching and red shift of themaximumwavelength of emission in a concentrationdependent manner showed that morin and scopoletin bind to LDH and affect its structure. Conclusions: The results suggest that morin and scopoletin bind to LDH, influence its conformation and inhibit its activity. Scopoletin showed more effective inhibition of LDH activity and it can be a promising candidate in the field of tumor metabolism inhibitors.
پژوهشگران	باقر سیدعلیپور (نفر سوم)، ملیحه سادات عطری (نفر دوم)، ملیکا مزلقانی نیا (نفر اول)